The muraminomicin biosynthetic gene cluster and enzymatic formation of the 2-deoxyaminoribosyl appendage.
The muraminomicin biosynthetic gene cluster and enzymatic formation of the 2-deoxyaminoribosyl appendage.
复制标题
DOI：
10.1039/c2md20245j
复制
发表时间：
2013-01-01
期刊：
影响因子：
--
通讯作者：
Van Lanen SG
中科院分区：
文献类型：
--
作者：
Chi X;Baba S;Tibrewal N;Funabashi M;Nonaka K;Van Lanen SG
Muraminomicin是由Streptosporangium amethystogenes SANK 60709产生的脂肽基核苷抗生素。与该抗生素家族的几个成员（如A-90289和Muraymycin）相似，胞壁霉素的结构由一个二糖组成，该二糖由两个通过O-β（1 → 5）糖苷键连接的修饰的呋喃核糖单元组成;然而，胞壁霉素的区别在于两个核糖单元都是2-脱氧糖。已经鉴定、克隆和测序了胞壁霉素的生物合成基因簇，生物信息学分析显示至少24个开放阅读框参与胞壁霉素的生物合成、抗性和调控。5种酶可能参与2，5-二脱氧-5-氨基核糖糖单元的组装和附着，其中2种酶的功能已确定并鉴定：Mra 20，一种5′-氨基-2 ′，5 ′-二脱氧尿苷磷酸化酶和Mra 23，一种UTP：5-氨基-2，5-二脱氧-α-D-核糖-1-磷酸尿苷酰转移酶。累积结果与通过与A-90289生物合成平行的典型糖生物合成途径掺入胞壁霉素的核糖基附件一致，并且该附件的特异性主要由两种表征的酶决定。
Muraminomicin is a lipopeptidyl nucleoside antibiotic produced by Streptosporangium amethystogenes SANK 60709. Similar to several members of this antibiotic family such as A-90289 and muraymycin, the structure of muraminomicin consists of a disaccharide comprised of two modified ribofuranose units linked by an O-β(1 → 5) glycosidic bond; however, muraminomicin holds the distinction in that both ribose units are 2-deoxy sugars. The biosynthetic gene cluster of muraminomicin has been identified, cloned and sequenced, and bioinformatic analysis revealed a minimum of 24 open reading frames putatively involved in the biosynthesis, resistance, and regulation of muraminomicin. Fives enzymes are likely involved in the assembly and attachment of the 2,5-dideoxy-5-aminoribose saccharide unit, and two are now functionally assigned and characterized: Mra20, a 5′-amino-2′,5′-dideoxyuridine phosphorylase and Mra23, a UTP:5-amino-2,5-dideoxy-α-D-ribose-1-phosphate uridylyltransferase. The cumulative results are consistent with the incorporation of the ribosyl appendage of muraminomicin via the archetypical sugar biosynthetic pathway that parallels A-90289 biosynthesis, and the specificity for this appendage is dictated primarily by the two characterized enzymes.